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Crystal Structure of the Di-Zinc Metallo-beta-lactamase VIM-4 from Pseudomonas aeruginosaCrystal Structure of the Di-Zinc Metallo-beta-lactamase VIM-4 from Pseudomonas aeruginosa
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe metallo-beta-lactamase VIM-4, mainly found in Pseudomonas aeruginosa or Acinetobacter baumannii was produced in Escherichia coli and characterized by biochemical and X-ray techniques. A detailed kinetic study performed in the presence of Zn(2+) concentration ranging from 0.4 to 100 muM showed that VIM-4 exhibits a kinetic profile similar to those of VIM-2 and VIM-1. However, VIM-4 is more active than VIM-1 against benzylpenicillin, cephalothin, nitrocefin and imipenem and less active than VIM-2 against ampicillin and meropenem. The crystal structure of the di-zinc form of VIM-4 was solved at 1.9 A. The sole difference between VIM-4 and VIM-1 is found at residue 228 which is Ser in VIM-1 and Arg in VIM-4. This substitution has a major impact on the VIM-4 catalytic efficiency when compared to VIM-1. By contrast, the differences between VIM-2 and VIM-4 seem due to a different position of the "flapping loop" and two substitutions in loop 2. Study of the thermal stability and the activity of the holo- and apo-VIM-4 enzymes revealed that Zn(2+) ions have a pronounced stabilizing effect on the enzyme and are necessary for preserving the structure. Biochemical and Structural Characterization of the Subclass B1 Metallo-{beta}-Lactamase VIM-4.,Lassaux P, Traore DA, Loisel E, Favier A, Docquier JD, Sohier JS, Laurent C, Bebrone C, Frere JM, Ferrer JL, Galleni M Antimicrob Agents Chemother. 2010 Dec 13. PMID:21149620[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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